메뉴 건너뛰기




Volumn 38, Issue 7, 2005, Pages 625-631

Characterization of prolidase activity in erythrocytes from a patient with prolidase deficiency: Comparison with prolidase I and II purified from normal human erythrocytes

Author keywords

Erythrocyte; L , D Amino acids; Prolidase deficiency; Prolidase I and II

Indexed keywords

ALANINE; AMINO ACID; DEXTRO ALANINE; DEXTRO LEUCINE; DEXTRO SERINE; DEXTRO VALINE; DIPEPTIDE; GLYCINE; GLYCYLPROLINE; IMINE; ISOLEUCINE; LEUCINE; METHIONYLPROLINE; PROLINE DIPEPTIDASE; PROLINE DIPEPTIDASE I; PROLINE DIPEPTIDASE II; UNCLASSIFIED DRUG; VALINE;

EID: 21844444110     PISSN: 00099120     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clinbiochem.2005.03.007     Document Type: Article
Times cited : (11)

References (24)
  • 1
    • 0001387530 scopus 로고
    • On proteolytic enzymes: IXX. Regarding the specificity of amino peptidase and carboxypeptidase: A new type of enzyme in the intestinal tract
    • M. Bergmann, and S.J. Fruton On proteolytic enzymes: IXX. Regarding the specificity of amino peptidase and carboxypeptidase: a new type of enzyme in the intestinal tract J. Biol. Chem. 117 1937 189 202
    • (1937) J. Biol. Chem. , vol.117 , pp. 189-202
    • Bergmann, M.1    Fruton, S.J.2
  • 2
    • 0014513044 scopus 로고
    • Molecular size estimates of human peptidases determined by separate gene loci
    • W.H. Lewis, and H. Harris Molecular size estimates of human peptidases determined by separate gene loci Ann. Hum. Genet. 32 1969 317 322
    • (1969) Ann. Hum. Genet. , vol.32 , pp. 317-322
    • Lewis, W.H.1    Harris, H.2
  • 3
    • 0025295191 scopus 로고
    • Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency
    • A. Tanoue, F. Endo, and I. Matsuda Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency J. Biol. Chem. 265 1990 11306 11311
    • (1990) J. Biol. Chem. , vol.265 , pp. 11306-11311
    • Tanoue, A.1    Endo, F.2    Matsuda, I.3
  • 4
    • 0024583005 scopus 로고
    • Primary structure and gene localization of human prolidase
    • F. Endo, A. Tanoue, and H. Nakai Primary structure and gene localization of human prolidase J. Biol. Chem. 264 1989 4476 44781
    • (1989) J. Biol. Chem. , vol.264 , pp. 4476-44781
    • Endo, F.1    Tanoue, A.2    Nakai, H.3
  • 6
    • 0016258415 scopus 로고
    • A prolidase deficiency in man with iminopeptiduria
    • G.F. Powell, M.A. Rasco, and R.M. Maniscalco A prolidase deficiency in man with iminopeptiduria Metabolism 23 1974 505 513
    • (1974) Metabolism , vol.23 , pp. 505-513
    • Powell, G.F.1    Rasco, M.A.2    Maniscalco, R.M.3
  • 7
    • 0017040602 scopus 로고
    • Studies on a patient with iminopeptiduria. I. Identification of urinary iminopeptides
    • H. Kodama, S. Umemura, and M. Shimomura Studies on a patient with iminopeptiduria. I. Identification of urinary iminopeptides Physiol. Chem. Phys. 8 1976 463 473
    • (1976) Physiol. Chem. Phys. , vol.8 , pp. 463-473
    • Kodama, H.1    Umemura, S.2    Shimomura, M.3
  • 8
    • 0016591014 scopus 로고
    • Iminodipeptiduria: A genetic defect in recycling collagen; A method for determining prolidase in erythrocytes
    • S.H. Jackson, A.W. Dennis, and M. Greenberg Iminodipeptiduria: a genetic defect in recycling collagen; a method for determining prolidase in erythrocytes Can. Med. Assoc. J. 113 1975 759 763
    • (1975) Can. Med. Assoc. J. , vol.113 , pp. 759-763
    • Jackson, S.H.1    Dennis, A.W.2    Greenberg, M.3
  • 9
    • 0017386359 scopus 로고
    • Prolidase deficiency: Report of a second case with quantitation of the excessively excreted amino acids
    • G.F. Powell, A. Kurosky, and R.M. Maniscalco Prolidase deficiency: report of a second case with quantitation of the excessively excreted amino acids J. Pediatr. 91 1977 242 246
    • (1977) J. Pediatr. , vol.91 , pp. 242-246
    • Powell, G.F.1    Kurosky, A.2    Maniscalco, R.M.3
  • 10
    • 0017752868 scopus 로고
    • Iminopeptiduria, skin ulcerations, and edema in a boy with prolidase deficiency
    • L.J. Sheffield, P. Schlesinger, and K. Faull Iminopeptiduria, skin ulcerations, and edema in a boy with prolidase deficiency J. Pediatr. 91 1977 578 583
    • (1977) J. Pediatr. , vol.91 , pp. 578-583
    • Sheffield, L.J.1    Schlesinger, P.2    Faull, K.3
  • 11
    • 0018155659 scopus 로고
    • Studies on a patient with iminodipeptiduria: II. Lack of prolidase activity in blood cells
    • S. Umemura Studies on a patient with iminodipeptiduria: II. Lack of prolidase activity in blood cells Physiol. Chem. Phys. 10 1978 279 283
    • (1978) Physiol. Chem. Phys. , vol.10 , pp. 279-283
    • Umemura, S.1
  • 12
    • 0021272177 scopus 로고
    • Substrate specificity of manganese-activated prolidase in control and prolidase-deficient cultured skin fibroblasts
    • J. Butterworth, and D.A. Priestman Substrate specificity of manganese-activated prolidase in control and prolidase-deficient cultured skin fibroblasts J. Inherit. Metab. Dis. 7 1984 32 34
    • (1984) J. Inherit. Metab. Dis. , vol.7 , pp. 32-34
    • Butterworth, J.1    Priestman, D.A.2
  • 13
    • 0021592829 scopus 로고
    • Prolidase deficiency: Characteristics of human skin fibroblast prolidase using colorimetric and fluorimetric assays
    • D.A. Priestman, and J. Butterworth Prolidase deficiency: characteristics of human skin fibroblast prolidase using colorimetric and fluorimetric assays Clin. Chim. Acta 142 1984 263 271
    • (1984) Clin. Chim. Acta , vol.142 , pp. 263-271
    • Priestman, D.A.1    Butterworth, J.2
  • 14
    • 0022380556 scopus 로고
    • Presence in human cells and tissues of two prolidases and their alteration in prolidase deficiency
    • J. Butterworth, and D.A. Priestman Presence in human cells and tissues of two prolidases and their alteration in prolidase deficiency J. Inherit. Metab. Dis. 8 1985 193 197
    • (1985) J. Inherit. Metab. Dis. , vol.8 , pp. 193-197
    • Butterworth, J.1    Priestman, D.A.2
  • 15
    • 0024500138 scopus 로고
    • Characteristics and partial purification of prolidase and prolinase from leukocytes of a normal human and a patient with prolidase deficiency
    • H. Kodama, T. Ohhashi, and C. Ohba Characteristics and partial purification of prolidase and prolinase from leukocytes of a normal human and a patient with prolidase deficiency Clin. Chim. Acta 180 1989 65 72
    • (1989) Clin. Chim. Acta , vol.180 , pp. 65-72
    • Kodama, H.1    Ohhashi, T.2    Ohba, C.3
  • 16
    • 84995989827 scopus 로고
    • Characteristics of partially purified prolidase from erythrocytes of normal individuals, of two patients with prolidase deficiency, and of the patient's mother
    • T. Ohhashi, T. Ohno, J. Arata, and H. Kodama Characteristics of partially purified prolidase from erythrocytes of normal individuals, of two patients with prolidase deficiency, and of the patient's mother J. Clin. Biochem. Nutr. 5 1988 183 192
    • (1988) J. Clin. Biochem. Nutr. , vol.5 , pp. 183-192
    • Ohhashi, T.1    Ohno, T.2    Arata, J.3    Kodama, H.4
  • 17
    • 0023598492 scopus 로고
    • Effect of long preincubation on the two forms of human erythrocyte prolidase
    • I. Myara Effect of long preincubation on the two forms of human erythrocyte prolidase Clin. Chim. Acta 170 1987 263 270
    • (1987) Clin. Chim. Acta , vol.170 , pp. 263-270
    • Myara, I.1
  • 18
    • 0142028095 scopus 로고    scopus 로고
    • Characteristics of prolidase from the erythrocytes of normal humans and patients with prolidase deficiency and their mother
    • K. Nakayama, S. Awata, J. Zhang, H. Kaba, M. Manabe, and H. Kodama Characteristics of prolidase from the erythrocytes of normal humans and patients with prolidase deficiency and their mother Clin. Chem. Lab. Med. 41 2003 1323 1328
    • (2003) Clin. Chem. Lab. Med. , vol.41 , pp. 1323-1328
    • Nakayama, K.1    Awata, S.2    Zhang, J.3    Kaba, H.4    Manabe, M.5    Kodama, H.6
  • 20
    • 33749787148 scopus 로고
    • Photometric estimation of proline and ornithine
    • F.P. Chinard Photometric estimation of proline and ornithine J. Biol. Chem. 199 1952 91 95
    • (1952) J. Biol. Chem. , vol.199 , pp. 91-95
    • Chinard, F.P.1
  • 21
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • H. Lineweaver, and K. Burk The determination of enzyme dissociation constants J. Am. Chem. Soc. 56 1934 658 666
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, K.2
  • 23
    • 0022654780 scopus 로고
    • Effect of topical application of glycine and proline on recalcitrant leg ulcers of prolidase deficiency
    • J. Arata, K. Hatakenaka, and T. Oono Effect of topical application of glycine and proline on recalcitrant leg ulcers of prolidase deficiency Arch Dermatol. 122 1986 626 627
    • (1986) Arch Dermatol. , vol.122 , pp. 626-627
    • Arata, J.1    Hatakenaka, K.2    Oono, T.3
  • 24
    • 0024239885 scopus 로고
    • In situ activation of human erythrocyte prolidase: Potential for enzyme replacement therapy in prolidase deficiency
    • P. Hechtman, A. Richter, N. Corman, and Y.M. Leong In situ activation of human erythrocyte prolidase: potential for enzyme replacement therapy in prolidase deficiency Pediatr. Res. 24 1988 709 712
    • (1988) Pediatr. Res. , vol.24 , pp. 709-712
    • Hechtman, P.1    Richter, A.2    Corman, N.3    Leong, Y.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.